ID   QUEC_STRMK              Reviewed;         221 AA.
AC   B2FRM5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=7-cyano-7-deazaguanine synthase {ECO:0000255|HAMAP-Rule:MF_01633};
DE            EC=6.3.4.20 {ECO:0000255|HAMAP-Rule:MF_01633};
DE   AltName: Full=7-cyano-7-carbaguanine synthase {ECO:0000255|HAMAP-Rule:MF_01633};
DE   AltName: Full=PreQ(0) synthase {ECO:0000255|HAMAP-Rule:MF_01633};
DE   AltName: Full=Queuosine biosynthesis protein QueC {ECO:0000255|HAMAP-Rule:MF_01633};
GN   Name=queC {ECO:0000255|HAMAP-Rule:MF_01633}; OrderedLocusNames=Smlt3700;
OS   Stenotrophomonas maltophilia (strain K279a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=522373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K279a;
RX   PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA   Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA   Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA   Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA   Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA   Parkhill J., Thomson N.R., Avison M.B.;
RT   "The complete genome, comparative and functional analysis of
RT   Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT   resistance determinants.";
RL   Genome Biol. 9:R74.1-R74.13(2008).
CC   -!- FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7-
CC       deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
CC       {ECO:0000255|HAMAP-Rule:MF_01633}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-carboxy-7-deazaguanine + ATP + NH4(+) = 7-cyano-7-
CC         deazaguanine + ADP + H(+) + H2O + phosphate; Xref=Rhea:RHEA:27982,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:45075,
CC         ChEBI:CHEBI:61036, ChEBI:CHEBI:456216; EC=6.3.4.20;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01633};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01633};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01633};
CC   -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01633}.
CC   -!- SIMILARITY: Belongs to the QueC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01633}.
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DR   EMBL; AM743169; CAQ47115.1; -; Genomic_DNA.
DR   RefSeq; WP_012481067.1; NC_010943.1.
DR   AlphaFoldDB; B2FRM5; -.
DR   SMR; B2FRM5; -.
DR   STRING; 522373.Smlt3700; -.
DR   EnsemblBacteria; CAQ47115; CAQ47115; Smlt3700.
DR   KEGG; sml:Smlt3700; -.
DR   eggNOG; COG0603; Bacteria.
DR   HOGENOM; CLU_081854_1_1_6; -.
DR   OMA; QDPIKYV; -.
DR   OrthoDB; 1681374at2; -.
DR   UniPathway; UPA00391; -.
DR   Proteomes; UP000008840; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01995; ExsB; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01633; QueC; 1.
DR   InterPro; IPR018317; QueC.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR42914; PTHR42914; 1.
DR   Pfam; PF06508; QueC; 1.
DR   PIRSF; PIRSF006293; ExsB; 1.
DR   TIGRFAMs; TIGR00364; TIGR00364; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Metal-binding; Nucleotide-binding;
KW   Queuosine biosynthesis; Reference proteome; Zinc.
FT   CHAIN           1..221
FT                   /note="7-cyano-7-deazaguanine synthase"
FT                   /id="PRO_1000186640"
FT   BINDING         8..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT   BINDING         186
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT   BINDING         196
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT   BINDING         199
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
FT   BINDING         202
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01633"
SQ   SEQUENCE   221 AA;  22720 MW;  ACDA34481B226F0E CRC64;
     MKKAVVLLSG GMDSAAVIAM AQEQGFAVHA LSVRYGQRHT SELDAAARVA KAQGVVAHKI
     VDVDLRSIGG SALTDDIDVP EAGGAGIPVT YVPARNTIML SLALGWAEVL GANDIFCGVN
     AVDYSGYPDC RPEFVAAFQA LANLATKSGV EGAGIKVHAP LQFLSKGQIV SEGVRLGVDF
     GLTVSCYNAD ANGAACGHCD ACRLRAQGFA EAGVPDPTLY A